Antimicrobial peptides are a class of small (<100 residues) host defense peptides that induce selective membrane lytic activity against microbial pathogens.  The permeabilizing behavior of these diverse peptides has been commonly attributed to the formation of pores, and such pore formation has been categorized as barrel-stave, toroidal, or carpet-like. Using atomic force microscopy, the disruption of supported lipid bilayer patches by protegrin-1 has been studied in a concentration-dependent manner. PG-1 acts to lower the interfacial energy of the bilayer in a way similar to detergents, stabilizing pore formation. The intercalation of PG-1 into the bilayer results in structures beyond that of pore formation, giving rise to worm-like micelles at high peptide concentrations. The interaction depends not only on the charge of the peptide, but also on the composition and  state of the membrane. Antimicrobial peptides with structural differences, magainin-1 and aurein 1.1, exhibit a mechanistic commonality.

Mechanism of structural transformations   indcued by antimicrobial peptides in lipid membranes

243rd National Meeting (2012)

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